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Structure paper

TitleReverse hierarchical DED assembly in the cFLIP-procaspase-8 and cFLIP-procaspase-8-FADD complexes.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 8974, Year 2024
Publish dateOct 17, 2024
AuthorsChao-Yu Yang / Yi-Chun Tseng / Yi-Fan Tu / Bai-Jiun Kuo / Li-Chung Hsu / Chia-I Lien / You-Sheng Lin / Yin-Ting Wang / Yen-Chen Lu / Tsung-Wei Su / Yu-Chih Lo / Su-Chang Lin /
PubMed AbstractcFLIP, a master anti-apoptotic regulator, targets the FADD-induced DED complexes of procaspase-8 in death receptor and ripoptosome signaling pathways. Several tumor cells maintain relatively high ...cFLIP, a master anti-apoptotic regulator, targets the FADD-induced DED complexes of procaspase-8 in death receptor and ripoptosome signaling pathways. Several tumor cells maintain relatively high levels of cFLIP in achieving their immortality. However, understanding the three-dimensional regulatory mechanism initiated or mediated by elevated levels of cFLIP has been limited by the absence of the atomic coordinates for cFLIP-induced DED complexes. Here we report the crystal plus cryo-EM structures to uncover an unconventional mechanism where cFLIP and procaspase-8 autonomously form a binary tandem DED complex, independent of FADD. This complex gains the ability to recruit FADD, thereby allosterically modulating cFLIP assembly and partially activating caspase-8 for RIPK1 cleavage. Our structure-guided mutagenesis experiments provide critical insights into these regulatory mechanisms, elucidating the resistance to apoptosis and necroptosis in achieving immortality. Finally, this research offers a unified model for the intricate bidirectional hierarchy-based processes using multiprotein helical assembly to govern cell fate decisions.
External linksNat Commun / PubMed:39419969 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.09 - 3.97 Å
Structure data

39424

8yni

EMDB-39424, PDB-8yni:
Structure of the FADD/Caspase-8/cFLIP death effector domain assembly
Method: EM (single particle) / Resolution: 3.66 Å

39425

8ynk

EMDB-39425, PDB-8ynk:
Structure of the Caspase-8/cFLIP death effector domain assembly
Method: EM (single particle) / Resolution: 3.62 Å

39426

8ynl

EMDB-39426, PDB-8ynl:
Structure of the Caspase-8/cFLIP death effector domain assembly
Method: EM (single particle) / Resolution: 3.55 Å

39427

8ynm

EMDB-39427, PDB-8ynm:
Structure of the Caspase-8/cFLIP death effector domain assembly
Method: EM (single particle) / Resolution: 3.49 Å

39428

8ynn

EMDB-39428, PDB-8ynn:
Structure of the Caspase-8/cFLIP death effector domain assembly
Method: EM (single particle) / Resolution: 3.97 Å

PDB-8ym4:
Structure of Caspase-8/cFLIP death effector domain assembly
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

PDB-8ym5:
Structure of Caspase-8/cFLIP death effector domain assembly
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-8ym6:
Structure of Caspase-8/cFLIP death effector domain assembly
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-SE:
SELENIUM ATOM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsAPOPTOSIS / FADD / Caspase-8 / cFLIP / death effector domain / cellular FLICE-like inhibitory protein

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